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Analysis of oligomeric protein complexes in the chloroplast sub-proteome of nucleic acid-binding proteins from mustard reveals potential redox regulators of plastid gene expression

Authors

  • Yvonne Schröter,

    1. Junior Research Group, Institute of General Botany and Plant Physiology, Friedrich-Schiller-University Jena, Jena, Germany
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    • These authors contributed equally to this work.

  • Sebastian Steiner,

    1. Junior Research Group, Institute of General Botany and Plant Physiology, Friedrich-Schiller-University Jena, Jena, Germany
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    • These authors contributed equally to this work.

  • Kevin Matthäi,

    1. Junior Research Group, Institute of General Botany and Plant Physiology, Friedrich-Schiller-University Jena, Jena, Germany
    Current affiliation:
    1. Kevin Matth.ai, Qiagen GmbH, Hilden, Germany
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  • Thomas Pfannschmidt

    Corresponding author
    1. Junior Research Group, Institute of General Botany and Plant Physiology, Friedrich-Schiller-University Jena, Jena, Germany
    • Junior Research Group “Plant acclimation to environmental changes: Protein analysis by MS” at the Institute of General Botany and Plant Physiology, Department of Plant Physiology, Friedrich-Schiller-University of Jena, Dornburger Str. 159, 07743 Jena, Germany Fax: +49-3641-949-232
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    • These authors contributed equally to this work.

Errata

This article is corrected by:

  1. Errata: Erratum: Analysis of oligomeric protein complexes in the chloroplast sub-proteome of nucleic acid-binding proteins from mustard reveals potential redox regulators of plastid gene expression Volume 10, Issue 15, 2887, Article first published online: 27 July 2010

Abstract

Photosynthetic light quality acclimation in plants involves redox-controlled changes in plastid gene expression. To study proteins potentially involved in this regulation, we isolated low-abundant chloroplast nucleic acid-binding proteins from the crucifere mustard (Sinapis alba) and investigated if photosynthetic redox signals affect their composition and/or oligomeric structure. We purified chloroplasts from plants subjected to light quality shifts and applied organelle lysates to heparin-Sepharose chromatography followed by 2-D blue native PAGE. We studied accumulation and structure of oligomeric protein complexes and applied MS/MS to identify them. We found ten oligomeric protein complexes of higher order and eleven smaller protein complexes or spots including plastid-encoded RNA polymerase (PEP), plastid transcriptionally active chromosome proteins, RNA-binding proteins, ribosomal subunits and chaperones. A translation elongation factor was found to be the only protein displaying major differences in its amounts in response to the growth lights. Furthermore, we found a novel thioredoxin as a subunit of the PEP, a 2-Cys-peroxiredoxin complex and a (soluble) ferredoxin:NADP-oxido-reductase, which represent potential redox regulator of plastid gene expression. A T-DNA knock-out line of the thioredoxin from Arabidopsis exhibits a yellowish-pale phenotype, demonstrating that this novel PEP subunit is essential for proper plastid development.

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